Clarke married Christopher Clarke in 1973 with whom she would go on to have one son and one daughter.[1] He obtained a job in the United States and the family moved there. Since Clarke was unable to work as a teacher, through not having appropriate qualifications she decided to update her scientific knowledge through a Master of Science degree in applied biology, awarded in 1990 from the Georgia Institute of Technology. This experience made her decide to seek a career in research related to proteins.[10] She was subsequently awarded a Doctor of Philosophy degree in 1993 for investigations of Bacterial Ribonuclease (Barnase) from the University of Cambridge supervised by Alan Fersht.[2][3][11]
Jane Clarke is a distinguished biophysical chemist at the University of Cambridge. She is recognised internationally for her multidisciplinary studies that have advanced the understanding of protein folding and misfolding. She pioneered the application of protein engineering techniques together with single molecule force spectroscopy and simulations to investigate the effect of force on proteins. For this she was awarded the Biophysical Society U.S Genomics Award for Outstanding Investigator in the field of Single Molecule Biology in 2010; at the time, the only non-US and still the only female recipient of this prestigious award.[16]
Jane Clarke is distinguished for the rigorous physical chemistry approaches she has adapted and applied to understand protein folding and misfolding. Her fundamental studies revealed the presence of both parallel pathways and frustration in the energy landscape of apparently simple proteins. Most significantly, she has made very important advances in the study of multi-domain systems. From her discovery that aggregation and misfolding are determined by sequence similarity, through to her seminal studies combining force spectroscopy and protein engineering to elucidate mechanical unfolding energy landscapes, she has transformed our understanding of the evolution, folding and energetics of multidomain proteins.[17]
In 2021 she spoke about her career in the BBC Radio 4 programme The Life Scientific.[10]
↑Clarke, J; Fersht, A. R. (1993). "Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation". Biochemistry. 32 (16): 4322–9. doi:10.1021/bi00067a022. PMID8476861.
